Lentil Protein and Tannic Acid Interaction Limits <i>in Vitro</i> Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Boachie, Ruth T.; Okagu, Ogadimma D.; Abioye, Raliat O.; Hüttmann, Nico; Oliviero, Teresa; Capuano, Edoardo; Fogliano, Vincenzo; Udenigwe, Chibuike C.

doi:10.1021/acs.jafc.2c00197

Cited by 14 publications

(13 citation statements)

References 39 publications

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“…The maximum emission wavelength (λ max ) had red-shifted to longer wavelengths by 3–5 nm, which were accompanied by slight changes in the secondary structure of noncovalent samples (Figure B). This suggested that the increasing Lut concentration enhanced the unfolding degree of MP and microenvironment polarity of the Tyr residues, i.e., noncovalent molecular forces such as hydrogen bonds formed within the conjugates changed the structural properties of the protein and exposed more Tyr residues. A similar quenching effect has been previously reported. , …”

Section: Resultssupporting

confidence: 91%

“…The larger PSDs were consistent with the decreasing trend of surface hydrophobicity (Figure C). In addition, the covalent samples exhibited lower heterogeneity in PSD than that seen in the noncovalent samples; therefore, the covalent samples may exhibit better solution stability, considering that the increase in the particle-specific surface area may increase water–particle interactions …”

Section: Resultsmentioning

confidence: 99%

“…These results were consistent with those of a previous study that showed that chlorogenic acid enhanced β-lactoglobulin unfolding and aggregation. 46 The PSDs of the covalent samples showed an approximate monomodal manner for all the fortified samples with increasing concentration of Lut. In comparison with the PSDs of the noncovalent samples, the major peaks of covalent samples increased from 458 nm to approximately 615 nm with increasing Lut content, suggesting that the covalent modification had a stronger effect on the PSDs than that of noncovalent modification.…”

Section: Quantitation Of the Amount Of Lut Bound To Mpmentioning

confidence: 99%

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Comparisons between Myofibrillar Protein–Luteolin Conjugates Fabricated through Covalent and Noncovalent Modification

Zhang

2023

J. Agric. Food Chem.

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Protein−flavonoid conjugation is considered to effectively enhance the functionality of proteins, although how different binding modes affect the conformation and antioxidative properties of these conjugates has yet to be revealed. Herein, myofibrillar protein (MP)−luteolin (Lut) conjugates were noncovalently and covalently constructed using equivalent amounts of Lut (10.00, 20.11, and 69.60 μmol/g protein). Fluorescence quenching confirmed that hydrophobic interactions were the main forces in noncovalent MP−Lut conjugates and that the binding was entropy-driven. Liquid chromatography−tandem mass spectrometry results confirmed that Lut could be covalently grafted with MP after alkaline treatment. Proteomics analysis identified that most graft sites were located on the myosin subunits. Intriguingly, in vitro results showed that the antioxidant activity was barely affected by the MP−Lut binding modes. This work provides a theoretical basis for the application of MP−Lut noncovalent/covalent complexes as functional components.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Quantitation Of the Amount Of Lut Bound To Mpmentioning

confidence: 99%

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Comparisons between Myofibrillar Protein–Luteolin Conjugates Fabricated through Covalent and Noncovalent Modification

Zhang

2023

J. Agric. Food Chem.

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“…EWP hydrolysate (~5 µg of protein) were analyzed by nLC-MS/MS and the data was processed as previously described [ 49 ]. In brief, mass spectra were generated on an Orbitrap Fusin mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) coupled to an UltiMate 3000 nanoRSLC (Dionex, Thermo Fisher Scientific, Waltham, MA, USA).…”

Section: Methodsmentioning

confidence: 99%

Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin

Abioye

Acquah

Hsu

et al. 2022

Gels

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Egg white protein hydrolysate generated with pepsin was investigated for the presence of peptides with self-assembly and hydrogelation properties. Incubation of the hydrolysates for 16 h resulted in aggregates with significantly (p < 0.05) lower free amino nitrogen and sulfhydryl contents, and higher particle diameter and surface hydrophobicity compared to the hydrolysates. LC-MS/MS analysis of the aggregates resulted in identification of 429 ovalbumin-derived peptides, among which the top-six aggregation-prone peptides IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL were predicted using AGGRESCAN by analysis of the aggregation “Hot Spots”. NIFYCPIAIM had the highest thioflavin T fluorescence intensity, particle diameter (5611.3 nm), and polydispersity index (1.0) after 24 h, suggesting the formation of β-sheet structures with heterogeneous particle size distribution. Transmission electron microscopy of MMYQIGLF, and VYSFSLASRL demonstrated the most favorable peptide self-assembly, based on the formation of densely packed, intertwined fibrils. Rheological studies confirmed the viscoelastic and mechanical properties of the hydrogels, with IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, and VYSFSLASRL forming elastic solid hydrogels (tan δ < 1), while YCPIAIMSA and MMYQIGLF formed viscous liquid-like hydrogels (tan δ > 1). The results provide valuable insight into the influence of peptide sequence on hydrogelation and self-assembly progression, and prospects of food peptides in biomaterial applications.

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“…Due to interactions with proteins, these compounds, especially tannins, may disturb hydrolysis. Recently, Boachie et al [2022] have reported that the interaction of lentil proteins with tannic acid diminished the susceptibility of proteins to pepsin hydrolysis, as the enzyme had a limited access to the protein structure, which resulted in a modification of the profile of released peptides. On the other hand, phenolic compounds -as powerful antioxidants -contributed to antioxidant capacity of lentil flour subjected to simulated in vitro gastrointestinal proteolysis [Zhang & Chang, 2019].…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Capacity of Lentil Flour Hydrolysates Obtained with Pancreatin

Sulewska¹,

Rybarczyk-Płońska²,

Karamać³

2022

Pol. J. Food Nutr. Sci.

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Lentil is a valuable protein-rich crop, the health-promoting value of which can be further enhanced by its protein hydrolysis. In the present study, lentil flour was treated with pancreatin and the antioxidant capacity of the obtained hydrolysates with different degrees of hydrolysis (DH, 4-20%) was determined and compared with that of flour. The molecular weight (MW) distribution of the lentil proteins and their products of hydrolysis was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Size exclusion-high performance liquid chromatography (SE--HPLC) was deployed to show the profile of low MW compounds of the hydrolysates. Additionally, total phenolic contents were determined with the Folin-Ciocalteu's phenol reagent. The hydrolysates had higher antiradical activity against DPPH • , Trolox equivalent antioxidant capacity (TEAC) measured by the assay with ABTS •+ , ferric reducing antioxidant power (FRAP), and ability to bind Fe 2+ compared to lentil flour. Between the hydrolysates, the highest DPPH • scavenging activity (EC 50 of 0.298 mg/mL), TEAC (98.6 µmol Trolox/g), FRAP (109.2 µmol Fe 2+ /g), antioxidant capacity of lipid-soluble compounds (ACL) determined by photoluminescence method (4.32 µmol Trolox/g), and Fe 2+ chelating activity (80% at hydrolysate concentration of 0.3 mg/mL) were found for those with low DH (4-8%), which contained some subunits of proteins, polypeptides, and peptides with a wide MW range (0.556-66.0 kDa). The total phenolic content increased with increasing DH. In conclusion, the antioxidant capacity of lentil flour can be significantly improved by the limited hydrolysis of its proteins with pancreatin, as a result of the release of polypeptides and peptides with a wide range of MW. Thus modified lentil flour may be addressed and explored in future research as a functional food ingredient.

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Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Cited by 14 publications

References 39 publications

Comparisons between Myofibrillar Protein–Luteolin Conjugates Fabricated through Covalent and Noncovalent Modification

Comparisons between Myofibrillar Protein–Luteolin Conjugates Fabricated through Covalent and Noncovalent Modification

Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin

Antioxidant Capacity of Lentil Flour Hydrolysates Obtained with Pancreatin

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